Recombinant Bovine coronavirus Nucleoprotein (N) is produced in E.coli and contains the complete expression region spanning amino acids 1-448. The protein features a C-terminal 6xHis tag, which makes purification and detection more straightforward. SDS-PAGE analysis confirms the nucleoprotein is greater than 90% pure, suggesting it provides a high-quality reagent for research purposes. This product is intended for research use only, not for diagnostic or therapeutic applications.
The nucleoprotein of Bovine coronavirus appears to play a critical role in the virus's life cycle. It's primarily involved in packaging viral RNA and forming the ribonucleoprotein complex. As a key component in viral replication and assembly, it may represent an important target for studies examining viral pathogenesis and host-virus interactions. This protein is likely valuable for research aimed at understanding coronavirus biology and developing antiviral strategies.
Potential Applications
Note: The applications listed below are based on what we know about this protein's biological functions, published research, and experience from experts in the field. However, we haven't fully tested all of these applications ourselves yet. We'd recommend running some preliminary tests first to make sure they work for your specific research goals.
1. Antibody Development and Validation Studies
This full-length recombinant bovine coronavirus nucleoprotein can serve as an immunogen for generating polyclonal or monoclonal antibodies specific to BCoV N protein. The C-terminal 6xHis tag makes purification and immobilization for antibody screening assays more manageable. With >90% purity, it appears suitable for immunization protocols and subsequent antibody characterization experiments. Researchers might apply this protein in ELISA-based antibody validation assays to determine binding specificity and affinity.
2. Protein-Protein Interaction Studies
Pull-down assays could use the nucleoprotein to identify cellular or viral proteins that interact with BCoV N protein during infection. The C-terminal His-tag makes immobilization on nickel-affinity matrices simpler for capturing potential binding partners from cell lysates or viral protein preparations. Co-immunoprecipitation experiments may also validate specific protein interactions. Such studies would likely contribute to understanding the molecular mechanisms behind bovine coronavirus replication and pathogenesis.
3. Biochemical Characterization and Biophysical Analysis
Detailed biochemical characterization becomes possible with this recombinant protein, including molecular weight confirmation, thermal stability analysis, and protein folding studies. The high purity level appears to allow for reliable spectroscopic analyses such as circular dichroism to examine secondary structure content. Size exclusion chromatography might be applied to study oligomerization states and protein complex formation. These analyses would probably provide fundamental insights into the structural properties of bovine coronavirus nucleoprotein.
4. Comparative Coronavirus Research
The recombinant BCoV nucleoprotein could serve as a reference standard in comparative studies examining nucleoprotein sequences, structures, and properties across different coronavirus species. Cross-reactivity studies with antibodies raised against other coronavirus nucleoproteins may identify conserved epitopes. This protein might also prove useful in phylogenetic and evolutionary studies of coronavirus nucleoproteins through sequence and structural comparisons with related viral proteins.
